NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|4506887|ref|NP_003000|]
View 

selenoprotein W [Homo sapiens]

Protein Classification

SelT/SelW/SelH family protein( domain architecture ID 10020357)

SelT/SelW/SelH family protein is a selenoprotein that possesses a thioredoxin-like fold and a conserved CXXC or CxxU (U is selenocysteine) motif near the N terminus, suggesting a redox function

CATH:  3.40.30.10
Gene Ontology:  GO:0016020
SCOP:  4002953

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
CXXU_selWTH TIGR02174
selT/selW/selH selenoprotein domain; This model represents a domain found in both bacteria and ...
5-78 1.03e-30

selT/selW/selH selenoprotein domain; This model represents a domain found in both bacteria and animals, including animal proteins SelT, SelW, and SelH, all of which are selenoproteins. In a CXXC motif near the N-terminus of the domain, selenocysteine may replace the second Cys. Proteins with this domain may include an insert of about 70 amino acids. This model is broader than the current SelW model pfam05169 in Pfam.


:

Pssm-ID: 274013  Cd Length: 73  Bit Score: 102.75  E-value: 1.03e-30
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4506887     5 VRVVYCGAUGYKSKYLQLKKKLEDEFPGrLDICGEGTPQATGFFEVMVAGKLIHSKKKGDGYVDTESKFLKLVA 78
Cdd:TIGR02174  1 VEVEYCGSCGYKPRAAELKQALLEEFPD-LEIEGENTPPTTGAFEVEVNGQLVWSKLEGGGFPEPEELKQLIRD 73
 
Name Accession Description Interval E-value
CXXU_selWTH TIGR02174
selT/selW/selH selenoprotein domain; This model represents a domain found in both bacteria and ...
5-78 1.03e-30

selT/selW/selH selenoprotein domain; This model represents a domain found in both bacteria and animals, including animal proteins SelT, SelW, and SelH, all of which are selenoproteins. In a CXXC motif near the N-terminus of the domain, selenocysteine may replace the second Cys. Proteins with this domain may include an insert of about 70 amino acids. This model is broader than the current SelW model pfam05169 in Pfam.


Pssm-ID: 274013  Cd Length: 73  Bit Score: 102.75  E-value: 1.03e-30
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4506887     5 VRVVYCGAUGYKSKYLQLKKKLEDEFPGrLDICGEGTPQATGFFEVMVAGKLIHSKKKGDGYVDTESKFLKLVA 78
Cdd:TIGR02174  1 VEVEYCGSCGYKPRAAELKQALLEEFPD-LEIEGENTPPTTGAFEVEVNGQLVWSKLEGGGFPEPEELKQLIRD 73
Rdx pfam10262
Rdx family; This entry is an approximately 100 residue region of selenoprotein-T, conserved ...
5-75 1.63e-16

Rdx family; This entry is an approximately 100 residue region of selenoprotein-T, conserved from plants to humans. The protein binds to UDP-glucose:glycoprotein glucosyltransferase (UGTR), the endoplasmic reticulum (ER)-resident protein, which is known to be involved in the quality control of protein folding. Selenium (Se) plays an essential role in cell survival and most of the effects of Se are probably mediated by selenoproteins, including selenoprotein T. However, despite its binding to UGTR and that its mRNA is up-regulated in extended asphyxia, the function of the protein and hence of this region of it is unknown. Selenoprotein W contains selenium as selenocysteine in the primary protein structure and levels of this selenoprotein are affected by selenium.


Pssm-ID: 463032  Cd Length: 74  Bit Score: 67.17  E-value: 1.63e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4506887     5 VRVVYCGAUGYKSKYLQLKKKLEDEFPGRLdICGEGTPQATGFFEVMVAGKLIHSKKKGDGYVdtESKFLK 75
Cdd:pfam10262  2 VTIEYCTQCGWLLRAAWLAQELLSTFPDEL-GEVALIPGTGGAFEVTLDGELVWSRKEDGGFP--EPKELK 69
SelTWH_Campy NF041051
SelT/SelW/SelH family (seleno)protein, Campylobacterial type; Members of this family are ...
5-62 2.16e-06

SelT/SelW/SelH family (seleno)protein, Campylobacterial type; Members of this family are primarily (perhaps exclusively) selenoproteins, found in Campylobacter species such as C. lari, but also in members of several other lineages. The protein family is related to SelT, SelW, and SelH, and features a CXXU motif.


Pssm-ID: 468979  Cd Length: 70  Bit Score: 41.10  E-value: 2.16e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 4506887    5 VRVVYCGAUGYKSKYLQLKKKLEDEFPgrlDICGEGTPQATGFFEVMVAGKLIHSKKK 62
Cdd:NF041051  1 VSIEYCNSUNYLPRAARLADELLSKYP---DAEVELIPGSGGVFEVEVDGKLIFSKKE 55
 
Name Accession Description Interval E-value
CXXU_selWTH TIGR02174
selT/selW/selH selenoprotein domain; This model represents a domain found in both bacteria and ...
5-78 1.03e-30

selT/selW/selH selenoprotein domain; This model represents a domain found in both bacteria and animals, including animal proteins SelT, SelW, and SelH, all of which are selenoproteins. In a CXXC motif near the N-terminus of the domain, selenocysteine may replace the second Cys. Proteins with this domain may include an insert of about 70 amino acids. This model is broader than the current SelW model pfam05169 in Pfam.


Pssm-ID: 274013  Cd Length: 73  Bit Score: 102.75  E-value: 1.03e-30
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4506887     5 VRVVYCGAUGYKSKYLQLKKKLEDEFPGrLDICGEGTPQATGFFEVMVAGKLIHSKKKGDGYVDTESKFLKLVA 78
Cdd:TIGR02174  1 VEVEYCGSCGYKPRAAELKQALLEEFPD-LEIEGENTPPTTGAFEVEVNGQLVWSKLEGGGFPEPEELKQLIRD 73
Rdx pfam10262
Rdx family; This entry is an approximately 100 residue region of selenoprotein-T, conserved ...
5-75 1.63e-16

Rdx family; This entry is an approximately 100 residue region of selenoprotein-T, conserved from plants to humans. The protein binds to UDP-glucose:glycoprotein glucosyltransferase (UGTR), the endoplasmic reticulum (ER)-resident protein, which is known to be involved in the quality control of protein folding. Selenium (Se) plays an essential role in cell survival and most of the effects of Se are probably mediated by selenoproteins, including selenoprotein T. However, despite its binding to UGTR and that its mRNA is up-regulated in extended asphyxia, the function of the protein and hence of this region of it is unknown. Selenoprotein W contains selenium as selenocysteine in the primary protein structure and levels of this selenoprotein are affected by selenium.


Pssm-ID: 463032  Cd Length: 74  Bit Score: 67.17  E-value: 1.63e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4506887     5 VRVVYCGAUGYKSKYLQLKKKLEDEFPGRLdICGEGTPQATGFFEVMVAGKLIHSKKKGDGYVdtESKFLK 75
Cdd:pfam10262  2 VTIEYCTQCGWLLRAAWLAQELLSTFPDEL-GEVALIPGTGGAFEVTLDGELVWSRKEDGGFP--EPKELK 69
SelTWH_Campy NF041051
SelT/SelW/SelH family (seleno)protein, Campylobacterial type; Members of this family are ...
5-62 2.16e-06

SelT/SelW/SelH family (seleno)protein, Campylobacterial type; Members of this family are primarily (perhaps exclusively) selenoproteins, found in Campylobacter species such as C. lari, but also in members of several other lineages. The protein family is related to SelT, SelW, and SelH, and features a CXXU motif.


Pssm-ID: 468979  Cd Length: 70  Bit Score: 41.10  E-value: 2.16e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 4506887    5 VRVVYCGAUGYKSKYLQLKKKLEDEFPgrlDICGEGTPQATGFFEVMVAGKLIHSKKK 62
Cdd:NF041051  1 VSIEYCNSUNYLPRAARLADELLSKYP---DAEVELIPGSGGVFEVEVDGKLIFSKKE 55
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH