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Conserved domains on  [gi|110735411|ref|NP_001036079|]
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selenoprotein P precursor [Mus musculus]

Protein Classification

NADH-quinone oxidoreductase subunit L( domain architecture ID 10519082)

NADH-quinone oxidoreductase subunit L is a component of the NADH dehydrogenase I complex, which shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SelP_N pfam04592
Selenoprotein P, N terminal region; SelP is the only known eukaryotic selenoprotein that ...
 23-240 9.83e-127

Selenoprotein P, N terminal region; SelP is the only known eukaryotic selenoprotein that contains multiple selenocysteine (Sec) residues, and accounts for more than 50% of the selenium content of rat and human plasma. It is thought to be glycosylated. SelP may have antioxidant properties. It can attach to epithelial cells, and may protect vascular endothelial cells against peroxynitrite toxicity. The high selenium content of SelP suggests that it may be involved in selenium intercellular transport or storage. The promoter structure of bovine SelP suggest that it may be involved in countering heavy metal intoxication, and may also have a developmental function. The N-terminal region of SelP can exist independently of the C terminal region. Zebrafish selenoprotein Pb lacks the C terminal Sec-rich region, and a protein encoded by the rat SelP gene and lacking this region has also been reported. N-terminal region contains a conserved SecxxCys motif, which is similar to the CysxxCys found in thioredoxins. It is speculated that the N terminal region may adopt a thioredoxin fold and catalyze redox reactions. The N-terminal region also contains a His-rich region, which is thought to mediate heparin binding. Binding to heparan proteoglycans could account for the membrane binding properties of SelP. The function of the bacterial members of this family is uncharacterized.


:

Pssm-ID: 461363  Cd Length: 233  Bit Score: 364.07  E-value: 9.83e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735411   23 GQSSACYKAPEWYIGDQNPMLNSEGKVTVVALLQASUYLCLLQASRLEDLRIKLESQGYFNISYIVVNHQGSPSQLKHSH 102
Cdd:pfam04592   1 NQSRICKEPPAWSIGDQDPMTNSAGSVTVVALLQASUYFCLLQASRLEDLRVKLENQGLVNISYMVVNHQGAQSRAMYPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735411  103 LKKQVSEHIAVYRQEEDGIDVWTLLNGNKDDFLIYDRCGRLVYHLGLPYSFLTFPYVEEAIKIAYCEERCGNCNLTSLED 182
Cdd:pfam04592  81 LKRRVSEHIPVYQQEELQPDVWTLLNGNKDDFLIYDRCGRLTYHLGLPYSFLTFPYVEEAIKITYCKDKCGNCSLTTLED 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110735411  183 EDFCKTVTSATANKTAEPSEAHSHHKHHNKH---------GQEHLGSSKPSENQQPGPSETTLPPSG 240
Cdd:pfam04592 161 QDECSTVTKATVDKPAEPEPFTRHEHHHSHHqghqhhhphHHHHHGSNHHSESQQSGPGEPHHPPHS 227
SelP_C super family cl04616
Selenoprotein P, C terminal region; SelP is the only known eukaryotic selenoprotein that ...
 256-380 6.79e-67

Selenoprotein P, C terminal region; SelP is the only known eukaryotic selenoprotein that contains multiple selenocysteine (Sec) residues, and accounts for more than 50% of the selenium content of rat and human plasma. It is thought to be glycosylated. SelP may have antioxidant properties. It can attach to epithelial cells, and may protect vascular endothelial cells against peroxynitrite toxicity. The high selenium content of SelP suggests that it may be involved in selenium intercellular transport or storage. The promoter structure of bovine SelP suggest that it may be involved in countering heavy metal intoxication, and may also have a developmental function. The N terminal region always contains one Sec residue, and this is separated from the C terminal region (9-16 sec residues) by a histidine-rich sequence. The large number of Sec residues in the C-terminal portion of SelP suggest CC that it may be involved in selenium transport or storage. However, it is also possible that this region has a redox function.


The actual alignment was detected with superfamily member pfam04593:

Pssm-ID: 335847  Cd Length: 133  Bit Score: 208.00  E-value: 6.79e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735411  256 LESUDTTASEGLHLSLAQRKLURRGCINQLLCKLSKESEAAPSSCCCHCRHLIFEKSGSAIAUQCAENLPSLCSUQGLFA 335
Cdd:pfam04593   8 LENUDTPASEGLQLSLAQKKLURKRCINQLLCKLPKDSEAAPSSCCCHCRHLIFEKTGSAITUQCAENLPSLCSUQGLFA 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 110735411  336 EEKVTESCQCRSPPAAUQ-NQPMNPMEANPNUSUDNQTRKUKUHSN 380
Cdd:pfam04593  88 EENVTESCQURLPPAAUQaNQQLNPTEASPNUSUKNQAKKUKUPSN 133
 
Name Accession Description Interval E-value
SelP_N pfam04592
Selenoprotein P, N terminal region; SelP is the only known eukaryotic selenoprotein that ...
 23-240 9.83e-127

Selenoprotein P, N terminal region; SelP is the only known eukaryotic selenoprotein that contains multiple selenocysteine (Sec) residues, and accounts for more than 50% of the selenium content of rat and human plasma. It is thought to be glycosylated. SelP may have antioxidant properties. It can attach to epithelial cells, and may protect vascular endothelial cells against peroxynitrite toxicity. The high selenium content of SelP suggests that it may be involved in selenium intercellular transport or storage. The promoter structure of bovine SelP suggest that it may be involved in countering heavy metal intoxication, and may also have a developmental function. The N-terminal region of SelP can exist independently of the C terminal region. Zebrafish selenoprotein Pb lacks the C terminal Sec-rich region, and a protein encoded by the rat SelP gene and lacking this region has also been reported. N-terminal region contains a conserved SecxxCys motif, which is similar to the CysxxCys found in thioredoxins. It is speculated that the N terminal region may adopt a thioredoxin fold and catalyze redox reactions. The N-terminal region also contains a His-rich region, which is thought to mediate heparin binding. Binding to heparan proteoglycans could account for the membrane binding properties of SelP. The function of the bacterial members of this family is uncharacterized.


Pssm-ID: 461363  Cd Length: 233  Bit Score: 364.07  E-value: 9.83e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735411   23 GQSSACYKAPEWYIGDQNPMLNSEGKVTVVALLQASUYLCLLQASRLEDLRIKLESQGYFNISYIVVNHQGSPSQLKHSH 102
Cdd:pfam04592   1 NQSRICKEPPAWSIGDQDPMTNSAGSVTVVALLQASUYFCLLQASRLEDLRVKLENQGLVNISYMVVNHQGAQSRAMYPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735411  103 LKKQVSEHIAVYRQEEDGIDVWTLLNGNKDDFLIYDRCGRLVYHLGLPYSFLTFPYVEEAIKIAYCEERCGNCNLTSLED 182
Cdd:pfam04592  81 LKRRVSEHIPVYQQEELQPDVWTLLNGNKDDFLIYDRCGRLTYHLGLPYSFLTFPYVEEAIKITYCKDKCGNCSLTTLED 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110735411  183 EDFCKTVTSATANKTAEPSEAHSHHKHHNKH---------GQEHLGSSKPSENQQPGPSETTLPPSG 240
Cdd:pfam04592 161 QDECSTVTKATVDKPAEPEPFTRHEHHHSHHqghqhhhphHHHHHGSNHHSESQQSGPGEPHHPPHS 227
SelP_C pfam04593
Selenoprotein P, C terminal region; SelP is the only known eukaryotic selenoprotein that ...
 256-380 6.79e-67

Selenoprotein P, C terminal region; SelP is the only known eukaryotic selenoprotein that contains multiple selenocysteine (Sec) residues, and accounts for more than 50% of the selenium content of rat and human plasma. It is thought to be glycosylated. SelP may have antioxidant properties. It can attach to epithelial cells, and may protect vascular endothelial cells against peroxynitrite toxicity. The high selenium content of SelP suggests that it may be involved in selenium intercellular transport or storage. The promoter structure of bovine SelP suggest that it may be involved in countering heavy metal intoxication, and may also have a developmental function. The N terminal region always contains one Sec residue, and this is separated from the C terminal region (9-16 sec residues) by a histidine-rich sequence. The large number of Sec residues in the C-terminal portion of SelP suggest CC that it may be involved in selenium transport or storage. However, it is also possible that this region has a redox function.


Pssm-ID: 335847  Cd Length: 133  Bit Score: 208.00  E-value: 6.79e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735411  256 LESUDTTASEGLHLSLAQRKLURRGCINQLLCKLSKESEAAPSSCCCHCRHLIFEKSGSAIAUQCAENLPSLCSUQGLFA 335
Cdd:pfam04593   8 LENUDTPASEGLQLSLAQKKLURKRCINQLLCKLPKDSEAAPSSCCCHCRHLIFEKTGSAITUQCAENLPSLCSUQGLFA 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 110735411  336 EEKVTESCQCRSPPAAUQ-NQPMNPMEANPNUSUDNQTRKUKUHSN 380
Cdd:pfam04593  88 EENVTESCQURLPPAAUQaNQQLNPTEASPNUSUKNQAKKUKUPSN 133
 
Name Accession Description Interval E-value
SelP_N pfam04592
Selenoprotein P, N terminal region; SelP is the only known eukaryotic selenoprotein that ...
 23-240 9.83e-127

Selenoprotein P, N terminal region; SelP is the only known eukaryotic selenoprotein that contains multiple selenocysteine (Sec) residues, and accounts for more than 50% of the selenium content of rat and human plasma. It is thought to be glycosylated. SelP may have antioxidant properties. It can attach to epithelial cells, and may protect vascular endothelial cells against peroxynitrite toxicity. The high selenium content of SelP suggests that it may be involved in selenium intercellular transport or storage. The promoter structure of bovine SelP suggest that it may be involved in countering heavy metal intoxication, and may also have a developmental function. The N-terminal region of SelP can exist independently of the C terminal region. Zebrafish selenoprotein Pb lacks the C terminal Sec-rich region, and a protein encoded by the rat SelP gene and lacking this region has also been reported. N-terminal region contains a conserved SecxxCys motif, which is similar to the CysxxCys found in thioredoxins. It is speculated that the N terminal region may adopt a thioredoxin fold and catalyze redox reactions. The N-terminal region also contains a His-rich region, which is thought to mediate heparin binding. Binding to heparan proteoglycans could account for the membrane binding properties of SelP. The function of the bacterial members of this family is uncharacterized.


Pssm-ID: 461363  Cd Length: 233  Bit Score: 364.07  E-value: 9.83e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735411   23 GQSSACYKAPEWYIGDQNPMLNSEGKVTVVALLQASUYLCLLQASRLEDLRIKLESQGYFNISYIVVNHQGSPSQLKHSH 102
Cdd:pfam04592   1 NQSRICKEPPAWSIGDQDPMTNSAGSVTVVALLQASUYFCLLQASRLEDLRVKLENQGLVNISYMVVNHQGAQSRAMYPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735411  103 LKKQVSEHIAVYRQEEDGIDVWTLLNGNKDDFLIYDRCGRLVYHLGLPYSFLTFPYVEEAIKIAYCEERCGNCNLTSLED 182
Cdd:pfam04592  81 LKRRVSEHIPVYQQEELQPDVWTLLNGNKDDFLIYDRCGRLTYHLGLPYSFLTFPYVEEAIKITYCKDKCGNCSLTTLED 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110735411  183 EDFCKTVTSATANKTAEPSEAHSHHKHHNKH---------GQEHLGSSKPSENQQPGPSETTLPPSG 240
Cdd:pfam04592 161 QDECSTVTKATVDKPAEPEPFTRHEHHHSHHqghqhhhphHHHHHGSNHHSESQQSGPGEPHHPPHS 227
SelP_C pfam04593
Selenoprotein P, C terminal region; SelP is the only known eukaryotic selenoprotein that ...
 256-380 6.79e-67

Selenoprotein P, C terminal region; SelP is the only known eukaryotic selenoprotein that contains multiple selenocysteine (Sec) residues, and accounts for more than 50% of the selenium content of rat and human plasma. It is thought to be glycosylated. SelP may have antioxidant properties. It can attach to epithelial cells, and may protect vascular endothelial cells against peroxynitrite toxicity. The high selenium content of SelP suggests that it may be involved in selenium intercellular transport or storage. The promoter structure of bovine SelP suggest that it may be involved in countering heavy metal intoxication, and may also have a developmental function. The N terminal region always contains one Sec residue, and this is separated from the C terminal region (9-16 sec residues) by a histidine-rich sequence. The large number of Sec residues in the C-terminal portion of SelP suggest CC that it may be involved in selenium transport or storage. However, it is also possible that this region has a redox function.


Pssm-ID: 335847  Cd Length: 133  Bit Score: 208.00  E-value: 6.79e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735411  256 LESUDTTASEGLHLSLAQRKLURRGCINQLLCKLSKESEAAPSSCCCHCRHLIFEKSGSAIAUQCAENLPSLCSUQGLFA 335
Cdd:pfam04593   8 LENUDTPASEGLQLSLAQKKLURKRCINQLLCKLPKDSEAAPSSCCCHCRHLIFEKTGSAITUQCAENLPSLCSUQGLFA 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 110735411  336 EEKVTESCQCRSPPAAUQ-NQPMNPMEANPNUSUDNQTRKUKUHSN 380
Cdd:pfam04593  88 EENVTESCQURLPPAAUQaNQQLNPTEASPNUSUKNQAKKUKUPSN 133
 
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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